Flippase kinase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53739 (FPK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Flippase kinase 1
EC=2.7.11.1

Gene names

Name:	FPK1
Ordered Locus Names:	YNR047W
ORF Names:	N3449

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	893 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response. Ref.3 Ref.9 Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Down-regulated by YKP1 phosphorylation. This effect is counteracted in the presence of mannosyl-inositolphosphorylceramide (MIPC). Ref.11
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein Ref.4.
Post-translational modification	The N-terminal non-catalytic domain is phosphorylated by YPK1. Ref.11
Miscellaneous	Present with 752 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. KIN82 subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid transport Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of phospholipid translocation Inferred from genetic interaction Ref.9. Source: SGD protein autophosphorylation Inferred from direct assay Ref.11. Source: SGD response to pheromone Inferred from mutant phenotype Ref.3. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.4 Ref.9. Source: SGD plasma membrane Inferred from direct assay Ref.11. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.11. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 893

893

Flippase kinase 1

PRO_0000086154

Regions

Domain

496 – 777

282

Protein kinase

Domain

778 – 861

AGC-kinase C-terminal

Nucleotide binding

502 – 510

ATP By similarity

Sites

Active site

621

Proton acceptor By similarity

Binding site

525

ATP By similarity

Amino acid modifications

Modified residue

140

Phosphoserine Ref.10

Modified residue

175

Phosphoserine Ref.10

Modified residue

185

Phosphoserine Ref.10

Modified residue

200

Phosphoserine Ref.10

Modified residue

263

Phosphoserine Ref.10

Modified residue

300

Phosphoserine Ref.10

Modified residue

303

Phosphoserine Ref.10

Modified residue

335

Phosphothreonine Ref.10

Modified residue

339

Phosphoserine Ref.8 Ref.10

Modified residue

414

Phosphoserine Ref.7 Ref.10

Modified residue

426

Phosphoserine Ref.10

Modified residue

462

Phosphoserine Ref.10

Modified residue

674

Phosphothreonine Ref.10

Modified residue

676

Phosphoserine Ref.6 Ref.10

Modified residue

680

Phosphothreonine Ref.10

Modified residue

876

Phosphothreonine Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

P53739 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 26AF74EE956F80DB
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FASTA

893

100,546

        10         20         30         40         50         60 
MAGHHHEHEQ ERDHEQEHEH DSLQRPTTGS ERTRSISFSK LLTRSWKRNA SSSNNMSVSS 

        70         80         90        100        110        120 
VNLYSDPENS RESDHNNSGS EGQSSRFSKL KSMFQSGNSS KNASAHNSSQ SSLEGDSASS 

       130        140        150        160        170        180 
SSKLRYVKPM TSVANASPAS PPLSPTIPET DVLQTPKMVH IDQHEHEREH SNCGSPIMLS 

       190        200        210        220        230        240 
SSSFSPTVAR TGTGRRRSPS TPIMPSQNSN NSSSTSAIRP NNYRHHSGSQ GFSSNNPFRE 

       250        260        270        280        290        300 
RAGTVRSSNP YFAYQGLPTH AMSSHDLDEG FQPYANGSGI HFLSTPTSKT NSLTNTKNLS 

       310        320        330        340        350        360 
NLSLNEIKEN EEVQEFNNED FFFHDIPKDL SLKDTLNGSP SRGSSKSPTI TQTFPSIIVG 

       370        380        390        400        410        420 
FDNEYEEDNN NDKHDEKEEQ QTTTDNKTRN LSPTKQNGKA THPRIKIPLR RAASEPNGLQ 

       430        440        450        460        470        480 
LASATSPTSS SARKTSGSSN INDKIPGQSV PPPNSFFPQE PSPKISDFPE PRRSRRLRTK 

       490        500        510        520        530        540 
SFSNKFQDIM VGPQSFEKIR LLGQGDVGKV FLVREKKTNR VYALKVLSKD EMIKRNKIKR 

       550        560        570        580        590        600 
VLTEQEILAT SNHPFIVTLY HSFQSEDYLY LCMEYCMGGE FFRALQTRKT KCICEDDARF 

       610        620        630        640        650        660 
YASEVTAALE YLHLLGFIYR DLKPENILLH QSGHIMLSDF DLSIQAKDSK VPVVKGSAQS 

       670        680        690        700        710        720 
TLVDTKICSD GFRTNSFVGT EEYIAPEVIR GNGHTAAVDW WTLGILIYEM LFGFTPFKGD 

       730        740        750        760        770        780 
NTNETFTNIL KNEVSFPNNN EISRTCKDLI KKLLTKNESK RLGCKMGAAD VKKHPFFKKV 

       790        800        810        820        830        840 
QWSLLRNQEP PLIPVLSEDG YDFAKLSSNK KRQTSQDSHK HLDEQEKNMF EERVEYDDEV 

       850        860        870        880        890 
SEDDPFHDFN SMSLMEQDNN SMIYGNTNSY GKIAYTPNSN RSRSNSHRTF FKR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast." Burchett S.A., Scott A., Errede B., Dohlman H.G. J. Biol. Chem. 276:26472-26478(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, MASS SPECTROMETRY. Strain: ADR376.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, MASS SPECTROMETRY.
[9]	"Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry." Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K. Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-175; SER-185; SER-200; SER-263; SER-300; SER-303; THR-335; SER-339; SER-414; SER-426; SER-462; THR-674; SER-676; THR-680 AND THR-876, MASS SPECTROMETRY.
[11]	"A protein kinase network regulates the function of aminophospholipid flippases." Roelants F.M., Baltz A.G., Trott A.E., Fereres S., Thorner J. Proc. Natl. Acad. Sci. U.S.A. 107:34-39(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY YPK1, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71662 Genomic DNA. Translation: CAA96328.1. BK006947 Genomic DNA. Translation: DAA10588.1.
PIR	S63378.
RefSeq	NP_014445.1. NM_001183224.1.
3D structure databases
ProteinModelPortal	P53739.
SMR	P53739. Positions 420-854.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6427N.
IntAct	P53739. 5 interactions.
MINT	MINT-601192.
STRING	4932.YNR047W.
Proteomic databases
PaxDb	P53739.
PRIDE	P53739.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNR047W; YNR047W; YNR047W.
GeneID	855783.
KEGG	sce:YNR047W.
Organism-specific databases
CYGD	YNR047w.
SGD	S000005330. FPK1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104731.
KO	K08286.
OMA	YDDEVSE.
OrthoDB	EOG49PF6Z.
Gene expression databases
Genevestigator	P53739.
GermOnline	YNR047W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.30.29.30. 1 hit.
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR011993. PH_like_dom. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980256.

Entry information

Entry name

FPK1_YEAST

Accession

Primary (citable) accession number: P53739
Secondary accession number(s): D6W1M2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents